Protein cold adaptation: Role of physico-chemical parameters in adaptation of proteins to low temperatures

Ecogenomics and Adaptation Strategies of Southern Ocean Viral Communities

“…Previous studies have shown a direct correlation between a high MW and the number of cavities in globular proteins, which translates to a higher energetically unfavorable packing probability ( 61 ). While a poor correlation has been observed for psychrophilic enzymes ( 62 ), we propose that the lower MW observed for SO viral proteins could decrease erroneous packaging frequency in an environment where high salt concentrations and low temperatures have a direct impact on protein folding and kinetics ( 33 ). Several threads of evidence presented in this work suggest that genes related to protein folding (i.e., chaperonins), as well as the variants of core proteins with reduced hydrophobic cores and lower MW, are under positive selection in the SO virome.…”

Cytoprotective effects of antioxidant supplementation on mesenchymal stem cell therapy

“…These chemicals are also known as potent antinitrosants (Grebowski, Kazmierska, & Krokosz, 2013;Injac et al, 2013;Kovel et al, 2019;Shokrollahzade, Sharifi, Vaseghi, Faridounnia, & Jahandideh, 2015).…”

Some Clues about Enzymes from Psychrophilic Microorganisms

“…Thus, it is expected that psychrophilic enzymes have a greater structural flexibility to increase the catalytic rate constant, and a higher degree of conformational complementarity with substrates to allow a decrease in activation energy, when compared to mesophilic and thermophilic homologues [23]. In order to shed light on these fundamental issues and to be sure that significant differences emerge, several structural comparative studies have been performed on enzyme families belonging to psychrophiles, mesophiles and thermophiles [24][25][26][27][28][29][30][31][32][33][34][35]. Even though adaptation strategies are family-specific, the following common rules hold for psychrophilic proteins: (a) the structural differences between the folded states are small and subtle, notwithstanding large differences in thermal stability; (b) there are several charged residues on the surface of psychrophilic enzymes to increase solubility and flexibility, not the conformational stability; (c) the interior packing, on the average, does not change; (d) there is a higher percentage of tiny residues (i.e., Ala, Gly, Ser, and Thr), whose small side chains make psychrophilic enzymes less compact and more flexible than the mesophilic and thermophilic counterparts.…”